Use of activity-based probes to develop high throughput screening assays that can be performed in complex cell extracts

PLoS ONE

Volumn 5, Issue 8, 2010, Pages

  Deu, Edgar ^a   Yang, Zhimou ^a   Wang, Flora ^b   Klemba, Michael ^b   Bogyo, Matthew ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CELL EXTRACT; DIPEPTIDYL PEPTIDASE; DIPEPTIDYL PEPTIDASE I; LIVER EXTRACT; PROLINE; PROTEINASE; RHODAMINE; PROTEINASE INHIBITOR;

ACTIVITY BASED PROBE; ANIMAL CELL; ARTICLE; CELL LYSATE; CONTROLLED STUDY; COVALENT BOND; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HIGH THROUGHPUT SCREENING; MOLECULAR PROBE; NONHUMAN; PLASMODIUM FALCIPARUM; PROTEIN TARGETING; RAT; SENSITIVITY AND SPECIFICITY; ANIMAL; CYTOLOGY; DRUG ANTAGONISM; DRUG SCREENING; HUMAN; LIVER; METABOLISM; METHODOLOGY; MOLECULAR LIBRARY;

PLASMODIUM FALCIPARUM; RATTUS;

ANIMALS; CATHEPSIN C; CELL EXTRACTS; DRUG EVALUATION, PRECLINICAL; HIGH-THROUGHPUT SCREENING ASSAYS; HUMANS; LIVER; MOLECULAR PROBES; PLASMODIUM FALCIPARUM; PROTEASE INHIBITORS; RATS; SMALL MOLECULE LIBRARIES; SUBSTRATE SPECIFICITY;

EID: 77957855676     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011985     Document Type: Article

References (19)

1. Williams KP, Scott JE (2009) Enzyme assay design for high-throughput screening. Methods Mol Biol 565: 107-126.
2. Zock JM (2009) Applications of high content screening in life science research. Comb Chem High Throughput Screen 12: 870-876.
3. An WF, Tolliday N (2010) Cell-based assays for high-throughput screening. Mol Biotechnol 45: 180-186.
4. Rosse G, Kueng E, Page MG, Schauer-Vukasinovic V, Giller T, et al. (2000) Rapid identification of substrates for novel proteases using a combinatorial peptide library. J Comb Chem 2: 461-466.
5. Luciani N, de Rocquigny H, Turcaud S, Romieu A, Roques BP (2001) Highly sensitive and selective fluorescence assays for rapid screening of endothelinconverting enzyme inhibitors. Biochem J 356: 813-819.
6. Wakata A, Lee HM, Rommel P, Toutchkine A, Schmidt M, et al. (2010) Simultaneous fluorescent monitoring of proteasomal subunit catalysis. J Am Chem Soc 132: 1578-1582.
7. Berger AB, Vitorino PM, Bogyo M (2004) Activity-based protein profiling: applications to biomarker discovery, in vivo imaging and drug discovery. Am J Pharmacogenomics 4: 371-381.
8. Fonovic M, Bogyo M (2007) Activity based probes for proteases: applications to biomarker discovery, molecular imaging and drug screening. Curr Pharm Des 13: 253-261.
9. Bachovchin DA, Brown SJ, Rosen H, Cravatt BF (2009) Identification of selective inhibitors of uncharacterized enzymes by high-throughput screening with fluorescent activity-based probes. Nat Biotechnol 27: 387-394.
10. Deu E, Leyva MJ, Albrow V, Rice MJ, Ellman JA, et al. (2010) Functional studies of the Plasmodium falciparum dipeptidyl aminopeptidase I (DPAP1) using small molecule inhibitors and active site probes. Chemistry and Biology In Submission.
11. Klemba M, Gluzman I, Goldberg DE (2004) A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J Biol Chem 279: 43000-43007.
12. Arastu-Kapur S, Ponder EL, Fonovic UP, Yeoh S, Yuan F, et al. (2008) Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum. Nat Chem Biol 4: 203-213.
13. Yuan F, Verhelst SH, Blum G, Coussens LM, Bogyo M (2006) A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I/cathepsin C. J Am Chem Soc 128: 5616-5617.
14. Wang F KP, Deu E, Bibb B, Lauritzen C, Pedersen J, Bogyo M, Klemba M (2010) Definition of the catalytic role of dipeptidyl aminopeptidase 1 in hemoglobin catabolism in the Plasmodium falciparum food vacuole. Molecular and Biochemical Parasitology, In Submission.
15. Evans MJ, Cravatt BF (2006) Mechanism-based profiling of enzyme families. Chem Rev 106: 3279-3301.
16. Cravatt BF, Wright AT, Kozarich JW (2008) Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu Rev Biochem 77: 383-414.
17. Leytus SP, Melhado LL, Mangel WF (1983) Rhodamine-based compounds as fluorogenic substrates for serine proteinases. Biochem J 209: 299-307.
18. Liu J, Bhalgat M, Zhang C, Diwu Z, Hoyland B, et al. (1999) Fluorescent molecular probes V: a sensitive caspase-3 substrate for fluorometric assays. Bioorg Med Chem Lett 9: 3231-3236.
19. Greenbaum D, Medzihradszky KF, Burlingame A, Bogyo M (2000) Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem Biol 7: 569-581.